› 1pq7

X-ray diffraction
0.8Å resolution

Trypsin at 0.8 A, pH5 / borax

Released:
DOI: 10.2210/pdb1pq7/pdb
PDB entry 1pq7 coloured by chain, front view.
PDB entry 1pq7 coloured by chain, side view.
PDB entry 1pq7 coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis.
Schmidt A, Jelsch C, Ostergaard P, Rypniewski W, Lamzin VS
J Biol Chem 278 43357-62 (2003)
PMID: 12937176

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 22.2 KDa
Source organism: Fusarium oxysporum
UniProt:
  • Canonical: P35049 (Residues: 25-248; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand ARG 1 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P1
Unit cell:
a: 32.869Å b: 37.022Å c: 39.78Å
α: 102.89° β: 104.59° γ: 102.37°
R-values:
R R work R free
0.109 0.109 not available

Quick links

Citations

2 review citations

Neutron Laue macromolecular crystallography.
Meilleur et al. (2006)
1 more

11 mentions without citation

Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction.
Smith et al. (2008)
10 more